uroporphyrinogen-III C-methyltransferase [Salinivirga cyanobacteriivorans]
Protein Classification
uroporphyrinogen-III C-methyltransferase( domain architecture ID 10000225)
uroporphyrinogen-III C-methyltransferase catalyzes two sequential methylation reactions (on C2 and C7) of uroporphyrinogen-III (UROGEN) to yield precorrin-2
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| CysG | COG0007 | Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
11-244 | 2.28e-70 | ||||
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; Uroporphyrinogen-III methylase (siroheme synthase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis : Pssm-ID: 439778 [Multi-domain] Cd Length: 245 Bit Score: 216.09 E-value: 2.28e-70
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| Name | Accession | Description | Interval | E-value | ||||
| CysG | COG0007 | Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
11-244 | 2.28e-70 | ||||
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; Uroporphyrinogen-III methylase (siroheme synthase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 439778 [Multi-domain] Cd Length: 245 Bit Score: 216.09 E-value: 2.28e-70
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| SUMT | cd11642 | Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
15-244 | 4.06e-63 | ||||
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SUMT); SUMT is an enzyme of the cobalamin and siroheme biosynthetic pathway. It catalyzes the first of three steps leading to the formation of siroheme from uroporphyrinogen III; it transfers two methyl groups from S-adenosyl-L-methionine to the C-2 and C-7 atoms of uroporphyrinogen III to yield precorrin-2 via the intermediate formation of precorrin-1. Precorrin-2 is also a precursor for the biosynthesis of vitamin B12, coenzyme F430, siroheme and heme d1. This family includes proteins in which the SUMT domain is fused to other functional domains, such as to a uroporphyrinogen-III synthase domain to form bifunctional uroporphyrinogen-III methylase/uroporphyrinogen-III synthase, or to a dual function dehydrogenase-chelatase domain, as in the case of the multifunctional S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase/dehydrogenase/ferrochelatase CysG, which catalyzes all three steps that transform uroporphyrinogen III into siroheme. Pssm-ID: 381169 Cd Length: 228 Bit Score: 197.27 E-value: 4.06e-63
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| cobA_cysG_Cterm | TIGR01469 | uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
11-244 | 3.48e-53 | ||||
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with uroporphyrin-III C-methyltransferase activity. This enzyme catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). Cobalamin contains cobalt while siroheme contains iron. Siroheme is a cofactor for nitrite and sulfite reductases and therefore plays a role in cysteine biosynthesis; many members of this family are CysG, siroheme synthase, with an additional N-terminal domain and with additional oxidation and iron insertion activities. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin] Pssm-ID: 273643 Cd Length: 236 Bit Score: 172.02 E-value: 3.48e-53
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| PRK06136 | PRK06136 | uroporphyrinogen-III C-methyltransferase; |
15-241 | 6.66e-48 | ||||
uroporphyrinogen-III C-methyltransferase; Pssm-ID: 235711 Cd Length: 249 Bit Score: 158.84 E-value: 6.66e-48
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| TP_methylase | pfam00590 | Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
11-223 | 1.03e-44 | ||||
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase. Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 149.42 E-value: 1.03e-44
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| Name | Accession | Description | Interval | E-value | |||||
| CysG | COG0007 | Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
11-244 | 2.28e-70 | |||||
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; Uroporphyrinogen-III methylase (siroheme synthase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 439778 [Multi-domain] Cd Length: 245 Bit Score: 216.09 E-value: 2.28e-70
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| SUMT | cd11642 | Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
15-244 | 4.06e-63 | |||||
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SUMT); SUMT is an enzyme of the cobalamin and siroheme biosynthetic pathway. It catalyzes the first of three steps leading to the formation of siroheme from uroporphyrinogen III; it transfers two methyl groups from S-adenosyl-L-methionine to the C-2 and C-7 atoms of uroporphyrinogen III to yield precorrin-2 via the intermediate formation of precorrin-1. Precorrin-2 is also a precursor for the biosynthesis of vitamin B12, coenzyme F430, siroheme and heme d1. This family includes proteins in which the SUMT domain is fused to other functional domains, such as to a uroporphyrinogen-III synthase domain to form bifunctional uroporphyrinogen-III methylase/uroporphyrinogen-III synthase, or to a dual function dehydrogenase-chelatase domain, as in the case of the multifunctional S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase/dehydrogenase/ferrochelatase CysG, which catalyzes all three steps that transform uroporphyrinogen III into siroheme. Pssm-ID: 381169 Cd Length: 228 Bit Score: 197.27 E-value: 4.06e-63
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| cobA_cysG_Cterm | TIGR01469 | uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
11-244 | 3.48e-53 | |||||
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with uroporphyrin-III C-methyltransferase activity. This enzyme catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). Cobalamin contains cobalt while siroheme contains iron. Siroheme is a cofactor for nitrite and sulfite reductases and therefore plays a role in cysteine biosynthesis; many members of this family are CysG, siroheme synthase, with an additional N-terminal domain and with additional oxidation and iron insertion activities. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin] Pssm-ID: 273643 Cd Length: 236 Bit Score: 172.02 E-value: 3.48e-53
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| PRK06136 | PRK06136 | uroporphyrinogen-III C-methyltransferase; |
15-241 | 6.66e-48 | |||||
uroporphyrinogen-III C-methyltransferase; Pssm-ID: 235711 Cd Length: 249 Bit Score: 158.84 E-value: 6.66e-48
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| TP_methylase | pfam00590 | Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
11-223 | 1.03e-44 | |||||
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase. Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 149.42 E-value: 1.03e-44
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| PLN02625 | PLN02625 | uroporphyrin-III C-methyltransferase |
15-244 | 2.31e-41 | |||||
uroporphyrin-III C-methyltransferase Pssm-ID: 178232 [Multi-domain] Cd Length: 263 Bit Score: 142.46 E-value: 2.31e-41
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| Precorrin-4_C11-MT | cd11641 | Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ... |
15-242 | 1.18e-38 | |||||
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. In the aerobic pathway, CobM catalyzes the methylation of precorrin-4 at C-11 to yield precorrin-5. In the anaerobic pathway, CibF catalyzes the methylation of cobalt-precorrin-4 to cobalt-precorrin-5. Both CibF and CobM, which are homologous, are included in this model. There are about 30 enzymes involved in vitamin B12 synthetic pathway. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared in both pathways and several of these enzymes are pathway-specific. Pssm-ID: 381168 [Multi-domain] Cd Length: 225 Bit Score: 134.44 E-value: 1.18e-38
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| cobM_cbiF | TIGR01465 | precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ... |
11-237 | 4.54e-37 | |||||
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-3B C17-methyltransferase, EC 2.1.1.131). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin] Pssm-ID: 200107 Cd Length: 247 Bit Score: 130.91 E-value: 4.54e-37
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| CobM | COG2875 | Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ... |
11-242 | 1.18e-35 | |||||
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 442122 [Multi-domain] Cd Length: 256 Bit Score: 127.48 E-value: 1.18e-35
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| cysG | PRK10637 | siroheme synthase CysG; |
11-226 | 4.34e-35 | |||||
siroheme synthase CysG; Pssm-ID: 182606 [Multi-domain] Cd Length: 457 Bit Score: 130.26 E-value: 4.34e-35
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| PRK07168 | PRK07168 | uroporphyrin-III C-methyltransferase; |
11-229 | 2.07e-24 | |||||
uroporphyrin-III C-methyltransferase; Pssm-ID: 180864 [Multi-domain] Cd Length: 474 Bit Score: 101.22 E-value: 2.07e-24
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| cbiF | PRK15473 | cobalt-precorrin-4 methyltransferase; |
15-223 | 3.96e-21 | |||||
cobalt-precorrin-4 methyltransferase; Pssm-ID: 185370 Cd Length: 257 Bit Score: 89.04 E-value: 3.96e-21
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| TP_methylase | cd11724 | uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
15-241 | 7.20e-21 | |||||
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily use S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and Ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide. Pssm-ID: 381178 [Multi-domain] Cd Length: 243 Bit Score: 88.00 E-value: 7.20e-21
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| TP_methylase | cd09815 | S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
15-223 | 2.12e-20 | |||||
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide. Pssm-ID: 381167 [Multi-domain] Cd Length: 219 Bit Score: 86.29 E-value: 2.12e-20
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| CobF | COG2243 | Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
11-223 | 2.46e-19 | |||||
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 441844 [Multi-domain] Cd Length: 229 Bit Score: 83.61 E-value: 2.46e-19
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| Precorrin_2_C20_MT | cd11645 | Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
15-217 | 3.68e-19 | |||||
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase (also known as S-adenosyl-L-methionine--precorrin-2 methyltransferase) participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. Precorrin-2 C20-methyltransferase catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 using S-adenosylmethionine as a methyl group source to produce precorrin-3A. In the anaerobic pathway, cobalt is inserted into precorrin-2 by CbiK to generate cobalt-precorrin-2, which is the substrate for CbiL, a C20 methyltransferase. In Clostridium difficile, CbiK and CbiL are fused into a bifunctional enzyme. In the aerobic pathway, the precorrin-2 C20-methyltransferase is named CobI. This family includes CbiL and CobI precorrin-2 C20-methyltransferases, both as stand-alone enzymes and when CbiL forms part of a bifunctional enzyme. Pssm-ID: 381172 [Multi-domain] Cd Length: 223 Bit Score: 82.94 E-value: 3.68e-19
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| cobI_cbiL | TIGR01467 | precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
11-215 | 8.06e-16 | |||||
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, one of several closely related S-adenosylmethionine-dependent methyltransferases involved in cobalamin (vitamin B12) biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin] Pssm-ID: 273642 [Multi-domain] Cd Length: 230 Bit Score: 74.27 E-value: 8.06e-16
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| cobJ_cbiH | TIGR01466 | precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ... |
11-222 | 9.81e-16 | |||||
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-4 C11-methyltransferase, EC 2.1.1.133). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. Members of this family may appear as fusion proteins with other enzymes of cobalamin biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin] Pssm-ID: 273641 [Multi-domain] Cd Length: 239 Bit Score: 73.87 E-value: 9.81e-16
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| PRK05787 | PRK05787 | cobalt-precorrin-7 (C(5))-methyltransferase; |
10-131 | 4.17e-15 | |||||
cobalt-precorrin-7 (C(5))-methyltransferase; Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 71.82 E-value: 4.17e-15
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| Precorrin-6Y-MT | cd11644 | Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
15-224 | 5.30e-15 | |||||
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also known as cobalt-precorrin-7 C(5)-methyltransferase, also known as cobalt-precorrin-6Y C(5)-methyltransferase) catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8. It participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. CbiE functions in the anaerobic pathway, it is a subunit of precorrin-6Y C5,15-methyltransferase, a bifunctional enzyme: cobalt-precorrin-7 C(5)-methyltransferase (CbiE)/cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (CbiT), that catalyzes two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. CbiE and CbiT can be found fused (CbiET, also called CobL), or on separate protein chains (CbiE and CbiT). In the aerobic pathway, a single enzyme called CobL catalyzes the methylations at C-5 and C-15, and the decarboxylation of the C-12 acetate side chain of precorrin-6B. Pssm-ID: 381171 [Multi-domain] Cd Length: 198 Bit Score: 71.37 E-value: 5.30e-15
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| Precorrin_3B_C17_MT | cd11646 | Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ... |
11-223 | 1.27e-14 | |||||
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17)-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model includes CobJ of the aerobic pathway and CbiH of the anaerobic pathway, both as stand-alone enzymes and when CobJ or CbiH form part of bifunctional enzymes, such as in Mycobacterium tuberculosis CobIJ where CobJ fuses with a precorrin-2 C(20)-methyltransferase domain, or Bacillus megaterium CbiH60, where CbiH is fused to a nitrite and sulfite reductase-like domain. In the aerobic pathway, once CobG has generated precorrin-3b, CobJ catalyzes the methylation of precorrin-3b at C-17 to form precorrin-4 (the extruded methylated C-20 fragment is left attached as an acyl group at C-1). In the corresponding anaerobic pathway, CbiH carries out this ring contraction, using cobalt-precorrin-3b as a substrate to generate a tetramethylated delta-lactone. Pssm-ID: 381173 [Multi-domain] Cd Length: 238 Bit Score: 70.91 E-value: 1.27e-14
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| CobJ | COG1010 | Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ... |
11-131 | 1.97e-14 | |||||
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 440634 Cd Length: 250 Bit Score: 70.48 E-value: 1.97e-14
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| CbiE | TIGR02467 | precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ... |
13-237 | 9.67e-13 | |||||
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes the CbiE methylase which is responsible, in part (along with CbiT), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiT subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. Pssm-ID: 274146 [Multi-domain] Cd Length: 204 Bit Score: 65.03 E-value: 9.67e-13
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| CobL | COG2241 | Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ... |
9-223 | 4.90e-12 | |||||
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 441842 [Multi-domain] Cd Length: 207 Bit Score: 63.24 E-value: 4.90e-12
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| PRK05765 | PRK05765 | precorrin-3B C17-methyltransferase; Provisional |
11-237 | 1.48e-11 | |||||
precorrin-3B C17-methyltransferase; Provisional Pssm-ID: 235597 Cd Length: 246 Bit Score: 62.49 E-value: 1.48e-11
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| PRK05576 | PRK05576 | cobalt-factor II C(20)-methyltransferase; |
15-216 | 1.95e-11 | |||||
cobalt-factor II C(20)-methyltransferase; Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 61.86 E-value: 1.95e-11
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| PRK05990 | PRK05990 | precorrin-2 C(20)-methyltransferase; Reviewed |
15-191 | 5.05e-09 | |||||
precorrin-2 C(20)-methyltransferase; Reviewed Pssm-ID: 180341 Cd Length: 241 Bit Score: 54.99 E-value: 5.05e-09
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| cbiH | PRK15478 | precorrin-3B C(17)-methyltransferase; |
13-131 | 2.61e-05 | |||||
precorrin-3B C(17)-methyltransferase; Pssm-ID: 185375 [Multi-domain] Cd Length: 241 Bit Score: 44.10 E-value: 2.61e-05
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| PRK05991 | PRK05991 | precorrin-3B C17-methyltransferase; Provisional |
11-131 | 1.95e-04 | |||||
precorrin-3B C17-methyltransferase; Provisional Pssm-ID: 180342 [Multi-domain] Cd Length: 250 Bit Score: 41.66 E-value: 1.95e-04
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| YabN_N_like | cd11723 | N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
11-39 | 7.82e-03 | |||||
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known. Pssm-ID: 381177 Cd Length: 218 Bit Score: 36.70 E-value: 7.82e-03
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